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Protein

ATP synthase subunit c, chloroplastic

Gene

atpH

Organism
Spinacia oleracea (Spinach)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

F1F0 ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F1 containing the extramembraneous catalytic core and F0 containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F1 is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
Key component of the F0 channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of 14 subunits forms the central stalk rotor element with the F1 delta and epsilon subunits.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei61 – 611Reversibly protonated during proton transportUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

ATP synthesis, Hydrogen ion transport, Ion transport, Transport

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

BRENDAi3.6.3.14. 5812.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP synthase subunit c, chloroplasticUniRule annotation
Alternative name(s):
ATP synthase F(0) sector subunit cUniRule annotation
ATPase subunit IIIUniRule annotation
F-type ATPase subunit cUniRule annotation
Short name:
F-ATPase subunit cUniRule annotation
Lipid-binding proteinUniRule annotation
Gene namesi
Name:atpHUniRule annotation
Encoded oniPlastid; Chloroplast
OrganismiSpinacia oleracea (Spinach)
Taxonomic identifieri3562 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeCaryophyllalesAmaranthaceaeChenopodioideaeAnserineaeSpinacia

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei3 – 2321HelicalUniRule annotationAdd
BLAST
Transmembranei57 – 7721HelicalUniRule annotationAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

CF(0), Chloroplast, Membrane, Plastid, Thylakoid

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL2366567.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 8181ATP synthase subunit c, chloroplasticPRO_0000112205Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-formylmethionine1 Publication

Keywords - PTMi

Formylation

Interactioni

Subunit structurei

F-type ATPases have 2 components, F1 - the catalytic core - and F0 - the membrane proton channel. F1 has five subunits: alpha3, beta3, gamma1, delta1, epsilon1. F0 has four main subunits: a1, b1, b'1 and c(14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F1 is attached to F0 by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta, b and b' chains.1 Publication

Structurei

Secondary structure

1
81
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 128
Helixi53 – 6513
Helixi69 – 757

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2W5JX-ray3.80A/B/C/D/E/F/G/H/I/J/K/L/M/V2-79[»]
ProteinModelPortaliP69447.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP69447.

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase C chain family.UniRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Family and domain databases

Gene3Di1.20.20.10. 1 hit.
HAMAPiMF_01396. ATP_synth_c_bact.
InterProiIPR000454. ATPase_F0-cplx_csu.
IPR005953. ATPase_F0-cplx_csu_bac/chlpt.
IPR020537. ATPase_F0-cplx_csu_DDCD_BS.
IPR002379. ATPase_proteolipid_c-like_dom.
[Graphical view]
PfamiPF00137. ATP-synt_C. 1 hit.
[Graphical view]
PRINTSiPR00124. ATPASEC.
SUPFAMiSSF81333. SSF81333. 1 hit.
TIGRFAMsiTIGR01260. ATP_synt_c. 1 hit.
PROSITEiPS00605. ATPASE_C. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P69447-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNPLIAAASV IAAGLAVGLA SIGPGVGQGT AAGQAVEGIA RQPEAEGKIR
60 70 80
GTLLLSLAFM EALTIYGLVV ALALLFANPF V
Length:81
Mass (Da):7,974
Last modified:July 21, 1986 - v1
Checksum:i75F8DBD4F23A896D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03775 Genomic DNA. Translation: CAA27402.1.
AJ400848 Genomic DNA. Translation: CAB88712.1.
PIRiS14423. LWSPA.
RefSeqiNP_054919.1. NC_002202.1.

Genome annotation databases

GeneIDi2715579.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03775 Genomic DNA. Translation: CAA27402.1.
AJ400848 Genomic DNA. Translation: CAB88712.1.
PIRiS14423. LWSPA.
RefSeqiNP_054919.1. NC_002202.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2W5JX-ray3.80A/B/C/D/E/F/G/H/I/J/K/L/M/V2-79[»]
ProteinModelPortaliP69447.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

ChEMBLiCHEMBL2366567.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi2715579.

Enzyme and pathway databases

BRENDAi3.6.3.14. 5812.

Miscellaneous databases

EvolutionaryTraceiP69447.
PROiP69447.

Family and domain databases

Gene3Di1.20.20.10. 1 hit.
HAMAPiMF_01396. ATP_synth_c_bact.
InterProiIPR000454. ATPase_F0-cplx_csu.
IPR005953. ATPase_F0-cplx_csu_bac/chlpt.
IPR020537. ATPase_F0-cplx_csu_DDCD_BS.
IPR002379. ATPase_proteolipid_c-like_dom.
[Graphical view]
PfamiPF00137. ATP-synt_C. 1 hit.
[Graphical view]
PRINTSiPR00124. ATPASEC.
SUPFAMiSSF81333. SSF81333. 1 hit.
TIGRFAMsiTIGR01260. ATP_synt_c. 1 hit.
PROSITEiPS00605. ATPASE_C. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Amino acid sequence of the proteolipid subunit of the ATP synthase from spinach chloroplasts."
    Sebald W., Wachter E.
    FEBS Lett. 122:307-311(1980)
    Cited for: PROTEIN SEQUENCE, FORMYLATION AT MET-1.
  2. "Localization and nucleotide sequence of the gene for the ATP synthase proteolipid subunit on the spinach plastid chromosome."
    Alt J., Winter P., Sebald W., Moser J.G., Schedel R., Westhoff P., Herrmann R.G.
    Curr. Genet. 7:129-138(1983)
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Chloroplast ATP synthase of spinach contains nine nonidentical subunit species, six of which are encoded by plastid chromosomes in two operons in a phylogenetically conserved arrangement."
    Hennig J., Herrmann R.G.
    Mol. Gen. Genet. 203:117-128(1986)
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "A gene cluster in the spinach and pea chloroplast genomes encoding one CF1 and three CF0 subunits of the H+-ATP synthase complex and the ribosomal protein S2."
    Hudson G.S., Mason J.G., Holton T.A., Koller B., Cox G.B., Whitfeld P.R., Bottomley W.
    J. Mol. Biol. 196:283-298(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "The plastid chromosome of spinach (Spinacia oleracea): complete nucleotide sequence and gene organization."
    Schmitz-Linneweber C., Maier R.M., Alcaraz J.-P., Cottet A., Herrmann R.G., Mache R.
    Plant Mol. Biol. 45:307-315(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Geant d'hiver and cv. Monatol.
  6. "Crystallization of the c14-rotor of the chloroplast ATP synthase reveals that it contains pigments."
    Varco-Merth B., Fromme R., Wang M., Fromme P.
    Biochim. Biophys. Acta 1777:605-612(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, PRELIMINARY CRYSTALLIZATION, PIGMENT COMPOSITION.

Entry informationi

Entry nameiATPH_SPIOL
AccessioniPrimary (citable) accession number: P69447
Secondary accession number(s): P00843, Q33180, Q9XPT1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: June 8, 2016
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

In plastids the F-type ATPase is also known as CF1CF0.

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.